Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5MLZ

Dolichyl phosphate mannose synthase in complex with GDP and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000271biological_processpolysaccharide biosynthetic process
A0004582molecular_functiondolichyl-phosphate beta-D-mannosyltransferase activity
A0005886cellular_componentplasma membrane
A0006486biological_processprotein glycosylation
A0006488biological_processdolichol-linked oligosaccharide biosynthetic process
A0006506biological_processGPI anchor biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0035269biological_processprotein O-linked mannosylation
A0046872molecular_functionmetal ion binding
A0180047biological_processdolichol phosphate mannose biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue GDP A 401
ChainResidue
APRO8
AASP89
AALA90
AASP91
AGLN93
AARG202
ASER207
ALYS208
AMG402
ATHR9
ATYR10
AGLU12
AVAL37
AASP39
AGLY68
ALEU69
AALA72

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
AASP91
AGLN93
AARG202
AGDP401

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 403
ChainResidue
AASN277
APHE301
AARG341

site_idAC4
Number of Residues5
Detailsbinding site for residue LDA A 404
ChainResidue
ASER243
AASN276
ATRP280
ATRP280
ATRP284

site_idAC5
Number of Residues4
Detailsbinding site for residue LDA A 405
ChainResidue
AGLU249
AGLY250
APHE251
ATRP253

site_idAC6
Number of Residues3
Detailsbinding site for residue LDA A 406
ChainResidue
ATRP317
AVAL343
AHIS347

site_idAC7
Number of Residues7
Detailsbinding site for residue LDA A 408
ChainResidue
AGLY244
AVAL270
ASER273
AASN277
ALEU306
ALEU306
ALDA409

site_idAC8
Number of Residues3
Detailsbinding site for residue LDA A 409
ChainResidue
AVAL270
AGLU271
ALDA408

site_idAC9
Number of Residues1
Detailsbinding site for residue LDA A 410
ChainResidue
ATYR222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues235
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues100
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28743912","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28743912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MLZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MM0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MM1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28743912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MM0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28743912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MM0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MM1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28743912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MLZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MM0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon